Results 81 to 90 of about 139,462,453 (100)

Elucidating metabolic pathways through genomic analysis in highly heavy metal-resistant <i>Halobacterium salinarum</i> strains. [PDF]

Heliyon
Baati H, Siala M, Benali S, Azri C, Dunlap C, Martínez-Espinosa RM, Trigui M.   +6 more
europepmc   +1 more source

Genome-wide high-density CRISPR interference screens reveal condition-specific metabolic vulnerabilities in Pseudomonas aeruginosa PAO1

Kaczmarczyk A, Klotz A, Manfredi P, Jenal U.   +3 more
europepmc   +1 more source

Structure of 2-Keto-3-Deoxy-6-Phosphogluconate (KDPG) Aldolase From Pseudomonas putida [PDF]

Acta Crystallographica Section D: Biological Crystallography, 2003
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida is a key enzyme in the Entner-Doudoroff pathway which catalyses the cleavage of KDPG via a class I Schiff-base mechanism. The crystal structure of this enzyme has been refined to a
Raghuvir K Arni, A Tulinsky, L Watanabe
exaly   +2 more sources

Slow-Binding Inhibition of 2-Keto-3-Deoxy-6-Phosphogluconate (KDPG) Aldolase

Bioorganic and Medicinal Chemistry, 2004
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase is a key enzyme in the Entner–Doudoroff pathway of bacteria. It catalyzes the reversible production of KDPG from pyruvate and -glyceraldehyde 3-phosphate through a class I Schiff base mechanism.
Laurence Hecquet, Casimir Blonski
exaly   +2 more sources

Cloning, Expression, Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase From Zymomonas mobilis ZM4 [PDF]

Acta Crystallographica Section F: Structural Biology Communications, 2010
Zymomonas mobilis ZM4 is an organism optimized for ethanol production which uses the Entner-Doudoroff (ED) pathway for the breakdown of glucose.
Sung Haeng Lee, Suk Youl Park, S Y Park
exaly   +2 more sources

Mechanism of the Class I KDPG Aldolase

Bioorganic and Medicinal Chemistry, 2006
In vivo, 2-keto-3-deoxy-6-pliosphogluconate (KDPG) aldolase catalyzes the reversible, stereospecific retro-aldol cleavage of KDPG to pyruvate and D-glyceraldehyde-3-phosphate. The enzyme is a lysine-dependent (Class 1) aldolase that functions through the
James Henderson Naismith, Carol A. Fierke, Eric Toone   +2 more
exaly   +2 more sources

Covalent Intermediate Trapped in 2-Keto-3-Deoxy-6- Phosphogluconate (KDPG) Aldolase Structure at 1.95-Å Resolution

Proceedings of the National Academy of Sciences of the United States of America, 2001
Jurgen Sygusch
exaly  

Directed Evolution of D-2-Keto-3-Deoxy-6-Phosphogluconate Aldolase to New Variants for the Efficient Synthesis of D- and L-Sugars

Chemistry and Biology, 2000
Chi-Huey Wong, S Fong
exaly  

Insights Into the Substrate Specificity of Archaeal Entner–Doudoroff Aldolases: The Structures of Picrophilus torridus 2-Keto-3-Deoxygluconate Aldolase and Sulfolobus solfataricus 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase in Complex With 2-Keto-3-Deoxy-6-Phosphogluconate

Biochemistry, 2018
Peter Schönheit, Susan J Crennell, Garry Taylor   +2 more
exaly  

Effect of Phosphorylation on the Reaction Rate of Unnatural Electrophiles With 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase

Journal of the Chemical Society, Perkin Transactions 1, 1998
Eric Toone
exaly